CAZyme Information: MGYG000004718_01031

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Anaerotignaceae; Anaerotignum
• CAZyme ID: MGYG000004718_01031
• CAZy Family: GT0
• CAZyme Description: UDP-N-acetylglucosamine 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
614		69224.26	4.5421

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004718	1910069	MAG	China	Asia

• Gene Location: Start: 5512; End: 7356 Strand: +

Full Sequence      

MNKIKVMSVFGTRPEAIKMAPLVKELEQTEEIESIVCVTAQHREMLDQVLEIFDLHPKHD
LNIMQSRQTLAGITTRALTGLETVIAEEKPDIVLVHGDTSTTFAGALAAYYNQVKVGHVE
AGLRTYDKYQPFPEEMNRCLTGTLTDLHFAPTALAKEHLLKENIAPESIFVTGNTVIDAL
AHTIEETYTFHESVLNTIDFAQKRVIAMTAHRRENLGEPLENICHAVKQIVDEFEDVEVV
YAVHKNPAVIEPVQRILGNHPRIHLTEPLDLKDMHNLMCRCYLVLTDSGGLQEEVPSMGK
PVLVLRNVTERPEGVEAGTLKLAGTEQQTIYTMTKTLLTDGTTYQQMAQAKNPFGDGNAS
KRIVQAILYAYGQTQQRPKDYIVTKSTANQTNKEAYYMKEERLAILSMLEKGLITVDEAE
RLLTVLQNGMGLEKDGIGKAVGNALEKAGDILGNVAKTMGEKAEQLQPKVKEVATKVADK
ADEMQPVVRSAVFRMTEKAHELKEDFKTYKEKMKNQKEEQEKEIYWDDEDEQELDADEAK
KEQDEQAENEIIENDPMIEKYAQNVEAVMHSVQQQMEQIDDAESFLKSAFGDVDPSEWED
DEDEQQQTDKNDTK

Enzyme Prediction     

No EC number prediction in MGYG000004718_01031.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0381	WecB	0.0	1	382	1	383	UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis].
TIGR00236	wecB	2.25e-177	4	371	1	365	UDP-N-acetylglucosamine 2-epimerase. This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
cd03786	GTB_UDP-GlcNAc_2-Epimerase	2.45e-164	5	368	1	365	UDP-N-acetylglucosamine 2-epimerase and similar proteins. Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
pfam02350	Epimerase_2	2.51e-151	24	368	1	336	UDP-N-acetylglucosamine 2-epimerase. This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional, in these instances Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of rat Gne is the kinase domain.
COG5281	COG5281	0.002	317	592	310	592	Phage-related minor tail protein [Mobilome: prophages, transposons].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCZ44502.1	1.92e-161	1	381	1	380
QGH21225.1	1.25e-159	1	381	1	380
ALP89282.1	1.25e-159	1	381	1	380
QJU45537.1	1.25e-159	1	381	1	380
AOR92965.1	1.25e-159	1	381	1	380

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4FKZ_A	6.78e-157	1	381	1	377	Crystalstructure of Bacillus subtilis UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP [Bacillus subtilis subsp. subtilis str. 168],4FKZ_B Crystal structure of Bacillus subtilis UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP [Bacillus subtilis subsp. subtilis str. 168]
3BEO_A	4.52e-154	2	368	7	370	AStructural Basis for the allosteric regulation of non-hydrolyzing UDP-GlcNAc 2-epimerases [Bacillus anthracis],3BEO_B A Structural Basis for the allosteric regulation of non-hydrolyzing UDP-GlcNAc 2-epimerases [Bacillus anthracis]
5ENZ_A	1.82e-153	5	381	3	375	S.aureus MnaA-UDP co-structure [Staphylococcus aureus],5ENZ_B S. aureus MnaA-UDP co-structure [Staphylococcus aureus]
1O6C_A	4.22e-150	2	381	2	377	Crystalstructure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis],1O6C_B Crystal structure of UDP-N-acetylglucosamine 2-epimerase [Bacillus subtilis]
3OT5_A	2.95e-146	1	383	25	403	2.2Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e],3OT5_B 2.2 Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e],3OT5_C 2.2 Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e],3OT5_D 2.2 Angstrom Resolution Crystal Structure of putative UDP-N-acetylglucosamine 2-epimerase from Listeria monocytogenes [Listeria monocytogenes EGD-e]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P45360	6.38e-159	1	381	1	381	Putative UDP-N-acetylglucosamine 2-epimerase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=CA_C2874 PE=3 SV=2
Q9X0C4	1.62e-157	4	372	2	369	Putative UDP-N-acetylglucosamine 2-epimerase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=TM_1034 PE=3 SV=1
P39131	2.81e-156	1	381	1	377	UDP-N-acetylglucosamine 2-epimerase OS=Bacillus subtilis (strain 168) OX=224308 GN=mnaA PE=1 SV=1
Q8XAR8	9.77e-123	4	367	1	369	UDP-N-acetylglucosamine 2-epimerase OS=Escherichia coli O157:H7 OX=83334 GN=wecB PE=3 SV=1
P58600	1.34e-122	5	367	3	370	Probable UDP-N-acetylglucosamine 2-epimerase OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=epsC PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004718_01031.